Open AccessMembrane potential independent binding of azidopyrene to LPS mutants of Salmonella typhimurium
Author(s) -
Wolf Marcia K.,
Konisky Jordan
Publication year - 1984
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1984.tb00186.x
Subject(s) - salmonella , mutant , membrane , chemistry , bacterial outer membrane , bacteria , biophysics , enterobacteriaceae , binding site , hydrophobic effect , cell membrane , microbiology and biotechnology , biochemistry , escherichia coli , biology , genetics , gene
The hydrophobic photoprobe azidopyrene has been used to probe the interaction of hydrophobic molecules with strains of Salmonella typhimurium carrying defined LPS mutations. We have found that whereas binding of this probe to cells having normal LPS is inversely related to the membrane potential (deenergized cells showed enhanced azidopyrene binding), mutants with defective LPS bind excess probe independent of the membrane potential. These results emphasize the role of LPS as a barrier to hydrophobic molecules.